Studies of phononlike low-energy excitations of protein molecules by inelastic x-ray scattering |
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Authors: | Liu Dazhi Chu Xiang-qiang Lagi Marco Zhang Yang Fratini Emiliano Baglioni Piero Alatas Ahmet Said Ayman Alp Ercan Chen Sow-Hsin |
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Affiliation: | Department of Nuclear Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA. |
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Abstract: | Molecular dynamics simulations and neutron scattering experiments have shown that many hydrated globular proteins exhibit a universal dynamic transition at TD = 220 K, below which the biological activity of a protein sharply diminishes. We studied the phononlike low-energy excitations of two structurally very different proteins, lysozyme and bovine serum albumin, using inelastic x-ray scattering above and below TD. We found that the excitation energies of the high-Q phonons show a marked softening above TD. This suggests that the large amplitude motions of wavelengths corresponding to this specific Q range are intimately correlated with the increase of biological activities of the proteins. |
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